WHITE_CERCA
ID WHITE_CERCA Reviewed; 679 AA.
AC Q17320;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein white;
GN Name=W;
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8533095; DOI=10.1126/science.270.5244.2005;
RA Zwiebel L.J., Saccone G., Zacharopoulou A., Besansky N.J., Favia G.,
RA Collins F.H., Louis C., Kafatos F.C.;
RT "The white gene of Ceratitis capitata: a phenotypic marker for germline
RT transformation.";
RL Science 270:2005-2007(1995).
CC -!- FUNCTION: May be part of a membrane-spanning permease system necessary
CC for the transport of pigment precursors into pigment cells responsible
CC for eye color.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR EMBL; X89933; CAA61998.1; -; mRNA.
DR RefSeq; NP_001266294.1; NM_001279365.1.
DR AlphaFoldDB; Q17320; -.
DR SMR; Q17320; -.
DR GeneID; 101458180; -.
DR KEGG; ccat:101458180; -.
DR CTD; 31271; -.
DR OrthoDB; 1022017at2759; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031409; F:pigment binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005284; Pigment_permease/Abcg.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00955; 3a01204; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Pigment;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..679
FT /note="Protein white"
FT /id="PRO_0000093381"
FT TRANSMEM 427..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 651..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 84..332
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 679 AA; 75145 MW; 3F9CBC78A835C4CC CRC64;
MGQEDQEVLI RGGKATSTSA ESLNNNNEQP YEQSSINQGF CKNYGTLSPP SPALTADNLT
YSWYNLDVFG AVHQPGSSWK QLVNRVKGVF CNERHIPAPR KHLLKNDSGV AYPGELLAVM
GSSGAGKTTL LNASAFRSSK GVQISPSTIR MLNGHPVDAK EMQARCAYVQ QDDLFIGSLT
AREHLIFQAM VRMPRHMTQK QKVQRVDQVI QDLSLGKCQN TLIGVPGRVK GLSGGERKRL
AFASEALTDP PLLICDEPTS GLDSFMAHSV VQVLKKLSQK GKTVILTIHQ PSSELFELFD
KILLMAEGRV AFLGTPGEAV DFFSYIGATC PTNYTPADFY VQVLAVVPGR EVESRDRVAK
ICDNFAVGKV SREMEQNFQK LVKSNGFGKE DENEYTYKAS WFMQFRAVLW RSWLSVLKEP
LLVKVRLLQT TMVAVLIGLI FLGQQLTQVG VMNINGAIFL FLTNMTFQNS FATITVFTTE
LPVFMRETRS RLYRCDTYFL GKTIAELPLF LVVPFLFTAI AYPLIGLRPG VDHFFTALAL
VTLVANVSTS FGYLISCACS STSMALSVGP PVIIPFLLFG GFFLNSGSVP VYFKWLSYLS
WFRYANEGLL INQWADVKPG EITCTLSNTT CPSSGEVILE TLNFSASDLP FDFIGLALLI
VGFRISAYIA LTMRARRKE